1M4R

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-22

Summary for 1M4R

• Entry DOI: 10.2210/pdb1m4r/pdb
• Descriptor: Interleukin-22 (2 entities in total)
• Functional Keywords: interleukin-22 (il-22), interleukin-10 (il-10), interferon-gamma, cytokines, cytokine
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: Q9GZX6
• Total number of polymer chains: 2
• Total formula weight: 34311.46

Authors

Nagem, R.A.P.,Colau, D.,Dumoutier, L.,Renauld, J.-C.,Ogata, C.,Polikarpov, I. (deposition date: 2002-07-03, release date: 2003-07-07, Last modification date: 2024-11-13)

Primary citation

Nagem, R.A.P.,Colau, D.,Dumoutier, L.,Renauld, J.-C.,Ogata, C.,Polikarpov, I.
Crystal Structure of Recombinant Human Interleukin-22
Structure, 10:1051-1062, 2002

PubMed Abstract: Interleukin-22 (IL-10-related T cell-derived inducible factor/IL-TIF/IL-22) is a novel cytokine belonging to the IL-10 family. Recombinant human IL-22 (hIL-22) was found to activate the signal transducers and activators of transcription factors 1 and 3 as well as acute phase reactants in several hepatoma cell lines, suggesting its involvement in the inflammatory response. The crystallographic structure of recombinant hIL-22 has been solved at 2.0 A resolution using the SIRAS method. Contrary to IL-10, the hIL-22 dimer does not present an interpenetration of the secondary-structure elements belonging to the two distinct polypeptide chains but results from interface interactions between monomers. Structural differences between these two cytokines, revealed by the crystallographic studies, clearly indicate that, while a homodimer of IL-10 is required for signaling, hIL-22 most probably interacts with its receptor as a monomer.

PubMed: 12176383
DOI: 10.1016/S0969-2126(02)00797-9

Experimental method

X-RAY DIFFRACTION (2 Å)